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Beschreibungen/Notizen
An NADPH-dependent pterocarpan synthase from elicitor-challenged soybean cell cultures was partially purified by a five-step procedure. The enzyme catalyses conversion of (3
R)2′-hydroxydihydrodaidzein to 3,9-dihydroxypterocarpan. Separation from NADPH: 2′-hydroxydaidzein oxidoreductase was achieved on Blue Sepharose. By gel filtration on Superose the
M
r
of pterocarpan synthase was shown to be
ca 29 000. The pH optimum of the reaction was 6.0. Apparent Michaelis constants for (
RS)2′-hydroxydihydrodaidzein and NADPH were, respectively, 75 and 45 μM. No reaction was observed with NADH. The enzyme was absent in extracts from soybean cells grown under standard conditions. With the glucan elicitor from
Phytophthora megasperma f. sp.
glycinea enzyme activity showed an increase up to 45 hr after challenge. Yeast extract caused only a transient increase in enzyme activity.